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Volumn 1817, Issue 6, 2012, Pages 928-937

Role of Surf1 in heme recruitment for bacterial COX biogenesis

Author keywords

Binuclear centre; Heme a; Heme incorporation; Heme copper oxidases; Oxidase biogenesis; Respiratory chain

Indexed keywords

ARGININE; BACTERIAL PROTEIN; CYTOCHROME C OXIDASE; FERROCHELATASE; FUNGAL PROTEIN; HEME; MITOCHONDRIAL PROTEIN; PROTEIN SHY1P; PROTEIN SURF1; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 84860699958     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2011.09.007     Document Type: Review
Times cited : (28)

References (77)
  • 1
    • 0029894544 scopus 로고    scopus 로고
    • Crosstalk between nuclear and mitochondrial genomes
    • R.O. Poyton, and J.E. McEwen Crosstalk between nuclear and mitochondrial genomes Annu. Rev. Biochem. 65 1996 563 607
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 563-607
    • Poyton, R.O.1    McEwen, J.E.2
  • 2
    • 0033766123 scopus 로고    scopus 로고
    • Human cytochrome oxidase deficiency
    • B.H. Robinson Human cytochrome oxidase deficiency Pediatr. Res. 48 2000 581 585
    • (2000) Pediatr. Res. , vol.48 , pp. 581-585
    • Robinson, B.H.1
  • 3
    • 0034951707 scopus 로고    scopus 로고
    • Cytochrome c oxidase deficiency
    • E.A. Shoubridge Cytochrome c oxidase deficiency Am. J. Med. Genet. 106 2001 46 52
    • (2001) Am. J. Med. Genet. , vol.106 , pp. 46-52
    • Shoubridge, E.A.1
  • 4
    • 29544449035 scopus 로고    scopus 로고
    • Biogenesis of cytochrome c oxidase
    • O. Khalimonchuk, and G. Rödel Biogenesis of cytochrome c oxidase Mitochondrion 5 2005 363 388
    • (2005) Mitochondrion , vol.5 , pp. 363-388
    • Khalimonchuk, O.1    Rödel, G.2
  • 5
    • 33947362946 scopus 로고    scopus 로고
    • Defects in cytochrome oxidase assembly in humans: Lessons from yeast
    • J.M. Zee, and D.M. Glerum Defects in cytochrome oxidase assembly in humans: lessons from yeast Biochem. Cell Biol. 84 2006 859 869
    • (2006) Biochem. Cell Biol. , vol.84 , pp. 859-869
    • Zee, J.M.1    Glerum, D.M.2
  • 6
    • 46349092291 scopus 로고    scopus 로고
    • Biogenesis of cytochrome c oxidase - In vitro approaches to study cofactor insertion into a bacterial subunit i
    • P. Greiner, A. Hannappel, C. Werner, and B. Ludwig Biogenesis of cytochrome c oxidase - in vitro approaches to study cofactor insertion into a bacterial subunit I Biochim. Biophys. Acta, Bioenerg. 1777 2008 904 911
    • (2008) Biochim. Biophys. Acta, Bioenerg. , vol.1777 , pp. 904-911
    • Greiner, P.1    Hannappel, A.2    Werner, C.3    Ludwig, B.4
  • 8
    • 0032760675 scopus 로고    scopus 로고
    • Expression and functional analysis of SURF1 in Leigh syndrome patients with cytochrome c oxidase deficiency
    • J. Yao, and E.A. Shoubridge Expression and functional analysis of SURF1 in Leigh syndrome patients with cytochrome c oxidase deficiency Hum. Mol. Genet. 8 1999 2541 2549
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 2541-2549
    • Yao, J.1    Shoubridge, E.A.2
  • 10
    • 0031009910 scopus 로고    scopus 로고
    • SHY1, the yeast homolog of the mammalian SURF-1 gene, encodes a mitochondrial protein required for respiration
    • G. Mashkevich, B. Repetto, D.M. Glerum, C. Jin, and A. Tzagoloff SHY1, the yeast homolog of the mammalian SURF-1 gene, encodes a mitochondrial protein required for respiration J. Biol. Chem. 272 1997 14356 14364
    • (1997) J. Biol. Chem. , vol.272 , pp. 14356-14364
    • Mashkevich, G.1    Repetto, B.2    Glerum, D.M.3    Jin, C.4    Tzagoloff, A.5
  • 11
    • 0000376151 scopus 로고
    • Subacute necrotizing encephalomyelopathy in an infant
    • D. Leigh Subacute necrotizing encephalomyelopathy in an infant J. Neurol. Neurosurg. Psychiatry 14 1951 216 221
    • (1951) J. Neurol. Neurosurg. Psychiatry , vol.14 , pp. 216-221
    • Leigh, D.1
  • 12
    • 0032750638 scopus 로고    scopus 로고
    • Sequence conservation from human to prokaryotes of Surf1, a protein involved in cytochrome c oxidase assembly, deficient in Leigh syndrome
    • A. Poyau, K. Buchet, and C. Godinot Sequence conservation from human to prokaryotes of Surf1, a protein involved in cytochrome c oxidase assembly, deficient in Leigh syndrome FEBS Lett. 462 1999 416 420
    • (1999) FEBS Lett. , vol.462 , pp. 416-420
    • Poyau, A.1    Buchet, K.2    Godinot, C.3
  • 13
    • 56349099660 scopus 로고    scopus 로고
    • Suppression mechanisms of COX assembly defects in yeast and human: Insights into the COX assembly process
    • A. Barrientos, K. Gouget, D. Horn, I.C. Soto, and F. Fontanesi Suppression mechanisms of COX assembly defects in yeast and human: insights into the COX assembly process Biochim. Biophys. Acta 1793 2009 97 107
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 97-107
    • Barrientos, A.1    Gouget, K.2    Horn, D.3    Soto, I.C.4    Fontanesi, F.5
  • 16
    • 4644319049 scopus 로고    scopus 로고
    • Mss51p and Cox14p jointly regulate mitochondrial Cox1p expression in Saccharomyces cerevisiae
    • A. Barrientos, A. Zambrano, and A. Tzagoloff Mss51p and Cox14p jointly regulate mitochondrial Cox1p expression in Saccharomyces cerevisiae EMBO J. 23 2004 3472 3482
    • (2004) EMBO J. , vol.23 , pp. 3472-3482
    • Barrientos, A.1    Zambrano, A.2    Tzagoloff, A.3
  • 17
    • 0242473137 scopus 로고    scopus 로고
    • Mss51p promotes mitochondrial Cox1p synthesis and interacts with newly synthesized Cox1p
    • X. Perez-Martinez, S.A. Broadley, and T.D. Fox Mss51p promotes mitochondrial Cox1p synthesis and interacts with newly synthesized Cox1p EMBO J. 22 2003 5951 5961
    • (2003) EMBO J. , vol.22 , pp. 5951-5961
    • Perez-Martinez, X.1    Broadley, S.A.2    Fox, T.D.3
  • 19
    • 35348842764 scopus 로고    scopus 로고
    • Coa1 links the Mss51 post-translational function to Cox1 cofactor insertion in cytochrome c oxidase assembly
    • F. Pierrel, M.L. Bestwick, P.A. Cobine, O. Khalimonchuk, J.A. Cricco, and D.R. Winge Coa1 links the Mss51 post-translational function to Cox1 cofactor insertion in cytochrome c oxidase assembly EMBO J. 26 2007 4335 4346
    • (2007) EMBO J. , vol.26 , pp. 4335-4346
    • Pierrel, F.1    Bestwick, M.L.2    Cobine, P.A.3    Khalimonchuk, O.4    Cricco, J.A.5    Winge, D.R.6
  • 20
    • 49449095848 scopus 로고    scopus 로고
    • Coa2 is an assembly factor for yeast cytochrome c oxidase biogenesis that facilitates the maturation of Cox1
    • F. Pierrel, O. Khalimonchuk, P.A. Cobine, M. Bestwick, and D.R. Winge Coa2 is an assembly factor for yeast cytochrome c oxidase biogenesis that facilitates the maturation of Cox1 Mol. Cell. Biol. 28 2008 4927 4939
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 4927-4939
    • Pierrel, F.1    Khalimonchuk, O.2    Cobine, P.A.3    Bestwick, M.4    Winge, D.R.5
  • 21
    • 40549085695 scopus 로고    scopus 로고
    • Transcriptional activators HAP/NF-Y rescue a cytochrome c oxidase defect in yeast and human cells
    • F. Fontanesi, C. Jin, A. Tzagoloff, and A. Barrientos Transcriptional activators HAP/NF-Y rescue a cytochrome c oxidase defect in yeast and human cells Hum. Mol. Genet. 17 2008 775 788
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 775-788
    • Fontanesi, F.1    Jin, C.2    Tzagoloff, A.3    Barrientos, A.4
  • 22
    • 52949096874 scopus 로고    scopus 로고
    • Two variants of the assembly factor Surf1 target specific terminal oxidases in Paracoccus denitrificans
    • F.A. Bundschuh, K. Hoffmeier, and B. Ludwig Two variants of the assembly factor Surf1 target specific terminal oxidases in Paracoccus denitrificans Biochim. Biophys. Acta 1777 2008 1336 1343
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 1336-1343
    • Bundschuh, F.A.1    Hoffmeier, K.2    Ludwig, B.3
  • 24
    • 0021767086 scopus 로고
    • Heme a induces assembly of rat liver cytochrome c oxidase subunits I-III in isolated mitochondria
    • A. Wielburski, and B.D. Nelson Heme a induces assembly of rat liver cytochrome c oxidase subunits I-III in isolated mitochondria FEBS Lett. 177 1984 291 294
    • (1984) FEBS Lett. , vol.177 , pp. 291-294
    • Wielburski, A.1    Nelson, B.D.2
  • 26
    • 0034711013 scopus 로고    scopus 로고
    • Identification of the structural subunits required for formation of the metal centers in subunit i of cytochrome c oxidase of Rhodobacter sphaeroides
    • M.R. Bratton, L. Hiser, W.E. Antholine, C. Hoganson, and J.P. Hosler Identification of the structural subunits required for formation of the metal centers in subunit I of cytochrome c oxidase of Rhodobacter sphaeroides Biochemistry 39 2000 12989 12995
    • (2000) Biochemistry , vol.39 , pp. 12989-12995
    • Bratton, M.R.1    Hiser, L.2    Antholine, W.E.3    Hoganson, C.4    Hosler, J.P.5
  • 27
    • 24044459731 scopus 로고    scopus 로고
    • Assembly of cytochrome-c oxidase in the absence of assembly protein Surf1p leads to loss of the active site heme
    • D. Smith, J. Gray, L. Mitchell, W.E. Antholine, and J.P. Hosler Assembly of cytochrome-c oxidase in the absence of assembly protein Surf1p leads to loss of the active site heme J. Biol. Chem. 280 2005 17652 17656
    • (2005) J. Biol. Chem. , vol.280 , pp. 17652-17656
    • Smith, D.1    Gray, J.2    Mitchell, L.3    Antholine, W.E.4    Hosler, J.P.5
  • 29
    • 70350033961 scopus 로고    scopus 로고
    • Surf1, associated with Leigh syndrome in humans, is a heme-binding protein in bacterial oxidase biogenesis
    • F.A. Bundschuh, A. Hannappel, O. Anderka, and B. Ludwig Surf1, associated with Leigh syndrome in humans, is a heme-binding protein in bacterial oxidase biogenesis J. Biol. Chem. 284 2009 25735 25741
    • (2009) J. Biol. Chem. , vol.284 , pp. 25735-25741
    • Bundschuh, F.A.1    Hannappel, A.2    Anderka, O.3    Ludwig, B.4
  • 30
    • 79955636958 scopus 로고    scopus 로고
    • Characterization of heme-binding properties of Paracoccus denitrificans Surf1 proteins
    • A. Hannappel, F.A. Bundschuh, and B. Ludwig Characterization of heme-binding properties of Paracoccus denitrificans Surf1 proteins FEBS J. 278 2011 1769 1778
    • (2011) FEBS J. , vol.278 , pp. 1769-1778
    • Hannappel, A.1    Bundschuh, F.A.2    Ludwig, B.3
  • 31
    • 0034641675 scopus 로고    scopus 로고
    • Self-assembly of heme A and heme B in a designed four-helix bundle: Implications for a cytochrome c oxidase maquette
    • B.R. Gibney, Y. Isogai, F. Rabanal, K.S. Reddy, A.M. Grosset, C.C. Moser, and P.L. Dutton Self-assembly of heme A and heme B in a designed four-helix bundle: implications for a cytochrome c oxidase maquette Biochemistry 39 2000 11041 11049
    • (2000) Biochemistry , vol.39 , pp. 11041-11049
    • Gibney, B.R.1    Isogai, Y.2    Rabanal, F.3    Reddy, K.S.4    Grosset, A.M.5    Moser, C.C.6    Dutton, P.L.7
  • 32
    • 59449101521 scopus 로고    scopus 로고
    • Regulation of the heme A biosynthetic pathway: Differential regulation of heme A synthase and heme O synthase in Saccharomyces cerevisiae
    • Z. Wang, Y. Wang, and E.L. Hegg Regulation of the heme A biosynthetic pathway: differential regulation of heme A synthase and heme O synthase in Saccharomyces cerevisiae J. Biol. Chem. 284 2009 839 847
    • (2009) J. Biol. Chem. , vol.284 , pp. 839-847
    • Wang, Z.1    Wang, Y.2    Hegg, E.L.3
  • 33
    • 0029930646 scopus 로고    scopus 로고
    • Low-spin heme A in the heme A biosynthetic protein CtaA from Bacillus subtilis
    • B. Svensson, K.K. Andersson, and L. Hederstedt Low-spin heme A in the heme A biosynthetic protein CtaA from Bacillus subtilis Eur. J. Biochem. 238 1996 287 295
    • (1996) Eur. J. Biochem. , vol.238 , pp. 287-295
    • Svensson, B.1    Andersson, K.K.2    Hederstedt, L.3
  • 34
    • 77955823775 scopus 로고    scopus 로고
    • Heme proteins - Diversity in structural characteristics, function, and folding
    • L.J. Smith, A. Kahraman, and J.M. Thornton Heme proteins - diversity in structural characteristics, function, and folding Proteins 78 2010 2349 2368
    • (2010) Proteins , vol.78 , pp. 2349-2368
    • Smith, L.J.1    Kahraman, A.2    Thornton, J.M.3
  • 35
    • 0033372003 scopus 로고    scopus 로고
    • Two novel mutations of SURF1 in Leigh syndrome with cytochrome c oxidase deficiency
    • M. Teraoka, Y. Yokoyama, S. Ninomiya, C. Inoue, S. Yamashita, and Y. Seino Two novel mutations of SURF1 in Leigh syndrome with cytochrome c oxidase deficiency Hum. Genet. 105 1999 560 563
    • (1999) Hum. Genet. , vol.105 , pp. 560-563
    • Teraoka, M.1    Yokoyama, Y.2    Ninomiya, S.3    Inoue, C.4    Yamashita, S.5    Seino, Y.6
  • 36
    • 77956700021 scopus 로고    scopus 로고
    • Analysis of Leigh syndrome mutations in the yeast SURF1 homolog reveals a new member of the cytochrome oxidase assembly factor family
    • M. Bestwick, M.Y. Jeong, O. Khalimonchuk, H. Kim, and D.R. Winge Analysis of Leigh syndrome mutations in the yeast SURF1 homolog reveals a new member of the cytochrome oxidase assembly factor family Mol. Cell. Biol. 30 2010 4480 4491
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 4480-4491
    • Bestwick, M.1    Jeong, M.Y.2    Khalimonchuk, O.3    Kim, H.4    Winge, D.R.5
  • 37
    • 79957493392 scopus 로고    scopus 로고
    • Mimicking a SURF1 allele reveals uncoupling of cytochrome c oxidase assembly from translational regulation in yeast
    • R. Reinhold, B. Bareth, M. Balleininger, M. Wissel, P. Rehling, and D.U. Mick Mimicking a SURF1 allele reveals uncoupling of cytochrome c oxidase assembly from translational regulation in yeast Hum. Mol. Genet. 20 2011 2379 2393
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 2379-2393
    • Reinhold, R.1    Bareth, B.2    Balleininger, M.3    Wissel, M.4    Rehling, P.5    Mick, D.U.6
  • 38
    • 0028890031 scopus 로고
    • Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans
    • S. Iwata, C. Ostermeier, B. Ludwig, and H. Michel Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans Nature 376 1995 660 669
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 39
    • 1542274547 scopus 로고    scopus 로고
    • Heme protein assemblies
    • C.J. Reedy, and B.R. Gibney Heme protein assemblies Chem. Rev. 104 2004 617 649
    • (2004) Chem. Rev. , vol.104 , pp. 617-649
    • Reedy, C.J.1    Gibney, B.R.2
  • 40
    • 0142154270 scopus 로고    scopus 로고
    • Mutations in COX10 result in a defect in mitochondrial heme A biosynthesis and account for multiple, early-onset clinical phenotypes associated with isolated COX deficiency
    • H. Antonicka, S.C. Leary, G.H. Guercin, J.N. Agar, R. Horvath, N.G. Kennaway, C.O. Harding, M. Jaksch, and E.A. Shoubridge Mutations in COX10 result in a defect in mitochondrial heme A biosynthesis and account for multiple, early-onset clinical phenotypes associated with isolated COX deficiency Hum. Mol. Genet. 12 2003 2693 2702
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 2693-2702
    • Antonicka, H.1    Leary, S.C.2    Guercin, G.H.3    Agar, J.N.4    Horvath, R.5    Kennaway, N.G.6    Harding, C.O.7    Jaksch, M.8    Shoubridge, E.A.9
  • 42
    • 0030802910 scopus 로고    scopus 로고
    • COX15 codes for a mitochondrial protein essential for the assembly of yeast cytochrome oxidase
    • D.M. Glerum, I. Muroff, C. Jin, and A. Tzagoloff COX15 codes for a mitochondrial protein essential for the assembly of yeast cytochrome oxidase J. Biol. Chem. 272 1997 19088 19094
    • (1997) J. Biol. Chem. , vol.272 , pp. 19088-19094
    • Glerum, D.M.1    Muroff, I.2    Jin, C.3    Tzagoloff, A.4
  • 43
    • 0028038276 scopus 로고
    • Isolation of a human cDNA for heme A:farnesyltransferase by functional complementation of a yeast cox10 mutant
    • D.M. Glerum, and A. Tzagoloff Isolation of a human cDNA for heme A:farnesyltransferase by functional complementation of a yeast cox10 mutant Proc. Natl Acad. Sci. USA 91 1994 8452 8456
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 8452-8456
    • Glerum, D.M.1    Tzagoloff, A.2
  • 44
    • 9644266771 scopus 로고    scopus 로고
    • Defects in the biosynthesis of mitochondrial heme c and heme a in yeast and mammals
    • C.T. Moraes, F. Diaz, and A. Barrientos Defects in the biosynthesis of mitochondrial heme c and heme a in yeast and mammals Biochim. Biophys. Acta 1659 2004 153 159
    • (2004) Biochim. Biophys. Acta , vol.1659 , pp. 153-159
    • Moraes, C.T.1    Diaz, F.2    Barrientos, A.3
  • 45
    • 0025076235 scopus 로고
    • COX10 codes for a protein homologous to the ORF1 product of Paracoccus denitrificans and is required for the synthesis of yeast cytochrome oxidase
    • M.P. Nobrega, F.G. Nobrega, and A. Tzagoloff COX10 codes for a protein homologous to the ORF1 product of Paracoccus denitrificans and is required for the synthesis of yeast cytochrome oxidase J. Biol. Chem. 265 1990 14220 14226
    • (1990) J. Biol. Chem. , vol.265 , pp. 14220-14226
    • Nobrega, M.P.1    Nobrega, F.G.2    Tzagoloff, A.3
  • 47
    • 33747453769 scopus 로고    scopus 로고
    • Heme: A versatile signaling molecule controlling the activities of diverse regulators ranging from transcription factors to MAP kinases
    • S.M. Mense, and L. Zhang Heme: a versatile signaling molecule controlling the activities of diverse regulators ranging from transcription factors to MAP kinases Cell Res. 16 2006 681 692
    • (2006) Cell Res. , vol.16 , pp. 681-692
    • Mense, S.M.1    Zhang, L.2
  • 48
    • 0037990786 scopus 로고    scopus 로고
    • Biogenesis of respiratory cytochromes in bacteria
    • L. Thony-Meyer Biogenesis of respiratory cytochromes in bacteria Microbiol. Mol. Biol. Rev. 61 1997 337 376
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 337-376
    • Thony-Meyer, L.1
  • 49
    • 0026740508 scopus 로고
    • Biologically relevant metal ion-dependent hydroxyl radical generation. An update
    • B. Halliwell, and J.M. Gutteridge Biologically relevant metal ion-dependent hydroxyl radical generation. An update FEBS Lett. 307 1992 108 112
    • (1992) FEBS Lett. , vol.307 , pp. 108-112
    • Halliwell, B.1    Gutteridge, J.M.2
  • 50
    • 0030008268 scopus 로고    scopus 로고
    • Fenton chemistry: An introduction
    • P. Wardman, and L.P. Candeias Fenton chemistry: an introduction Radiat. Res. 145 1996 523 531
    • (1996) Radiat. Res. , vol.145 , pp. 523-531
    • Wardman, P.1    Candeias, L.P.2
  • 51
    • 0037735344 scopus 로고    scopus 로고
    • Copper toxicity, oxidative stress, and antioxidant nutrients
    • L.M. Gaetke, and C.K. Chow Copper toxicity, oxidative stress, and antioxidant nutrients Toxicology 189 2003 147 163
    • (2003) Toxicology , vol.189 , pp. 147-163
    • Gaetke, L.M.1    Chow, C.K.2
  • 52
    • 33746929896 scopus 로고    scopus 로고
    • Copper trafficking to the mitochondrion and assembly of copper metalloenzymes
    • P.A. Cobine, F. Pierrel, and D.R. Winge Copper trafficking to the mitochondrion and assembly of copper metalloenzymes Biochim. Biophys. Acta 1763 2006 759 772
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 759-772
    • Cobine, P.A.1    Pierrel, F.2    Winge, D.R.3
  • 53
    • 4143074731 scopus 로고    scopus 로고
    • Specific copper transfer from the Cox17 metallochaperone to both Sco1 and Cox11 in the assembly of yeast cytochrome C oxidase
    • Y.C. Horng, P.A. Cobine, A.B. Maxfield, H.S. Carr, and D.R. Winge Specific copper transfer from the Cox17 metallochaperone to both Sco1 and Cox11 in the assembly of yeast cytochrome C oxidase J. Biol. Chem. 279 2004 35334 35340
    • (2004) J. Biol. Chem. , vol.279 , pp. 35334-35340
    • Horng, Y.C.1    Cobine, P.A.2    Maxfield, A.B.3    Carr, H.S.4    Winge, D.R.5
  • 54
    • 0034614510 scopus 로고    scopus 로고
    • Cox11p is required for stable formation of the Cu(B) and magnesium centers of cytochrome c oxidase
    • L. Hiser, M. Di Valentin, A.G. Hamer, and J.P. Hosler Cox11p is required for stable formation of the Cu(B) and magnesium centers of cytochrome c oxidase J. Biol. Chem. 275 2000 619 623
    • (2000) J. Biol. Chem. , vol.275 , pp. 619-623
    • Hiser, L.1    Di Valentin, M.2    Hamer, A.G.3    Hosler, J.P.4
  • 56
    • 0036671471 scopus 로고    scopus 로고
    • Cytochrome c maturation: A complex pathway for a simple task?
    • L. Thony-Meyer Cytochrome c maturation: a complex pathway for a simple task? Biochem. Soc. Trans. 30 2002 633 638
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 633-638
    • Thony-Meyer, L.1
  • 57
    • 18844469918 scopus 로고    scopus 로고
    • A heme chaperone for cytochrome c biosynthesis
    • L. Thony-Meyer A heme chaperone for cytochrome c biosynthesis Biochemistry 42 2003 13099 13105
    • (2003) Biochemistry , vol.42 , pp. 13099-13105
    • Thony-Meyer, L.1
  • 58
    • 6344282706 scopus 로고    scopus 로고
    • Heme O synthase and heme A synthase from Bacillus subtilis and Rhodobacter sphaeroides interact in Escherichia coli
    • B.M. Brown, Z. Wang, K.R. Brown, J.A. Cricco, and E.L. Hegg Heme O synthase and heme A synthase from Bacillus subtilis and Rhodobacter sphaeroides interact in Escherichia coli Biochemistry 43 2004 13541 13548
    • (2004) Biochemistry , vol.43 , pp. 13541-13548
    • Brown, B.M.1    Wang, Z.2    Brown, K.R.3    Cricco, J.A.4    Hegg, E.L.5
  • 59
    • 0037051889 scopus 로고    scopus 로고
    • Regulation of the heme A biosynthetic pathway in Saccharomyces cerevisiae
    • M.H. Barros, and A. Tzagoloff Regulation of the heme A biosynthetic pathway in Saccharomyces cerevisiae FEBS Lett. 516 2002 119 123
    • (2002) FEBS Lett. , vol.516 , pp. 119-123
    • Barros, M.H.1    Tzagoloff, A.2
  • 60
    • 0035831217 scopus 로고    scopus 로고
    • Involvement of mitochondrial ferredoxin and Cox15p in hydroxylation of heme O
    • M.H. Barros, C.G. Carlson, D.M. Glerum, and A. Tzagoloff Involvement of mitochondrial ferredoxin and Cox15p in hydroxylation of heme O FEBS Lett. 492 2001 133 138
    • (2001) FEBS Lett. , vol.492 , pp. 133-138
    • Barros, M.H.1    Carlson, C.G.2    Glerum, D.M.3    Tzagoloff, A.4
  • 61
    • 0025828687 scopus 로고
    • Bacillus subtilis expresses two kinds of haem-A-containing terminal oxidases
    • M. Lauraeus, T. Haltia, M. Saraste, and M. Wikstrom Bacillus subtilis expresses two kinds of haem-A-containing terminal oxidases Eur. J. Biochem. 197 1991 699 705
    • (1991) Eur. J. Biochem. , vol.197 , pp. 699-705
    • Lauraeus, M.1    Haltia, T.2    Saraste, M.3    Wikstrom, M.4
  • 63
    • 0035371783 scopus 로고    scopus 로고
    • A novel scenario for the evolution of haem-copper oxygen reductases
    • M.M. Pereira, M. Santana, and M. Teixeira A novel scenario for the evolution of haem-copper oxygen reductases Biochim. Biophys. Acta 1505 2001 185 208
    • (2001) Biochim. Biophys. Acta , vol.1505 , pp. 185-208
    • Pereira, M.M.1    Santana, M.2    Teixeira, M.3
  • 64
    • 77956543029 scopus 로고    scopus 로고
    • A novel heme a insertion factor gene cotranscribes with the Thermus thermophilus cytochrome ba3 oxidase locus
    • C. Werner, O.M. Richter, and B. Ludwig A novel heme a insertion factor gene cotranscribes with the Thermus thermophilus cytochrome ba3 oxidase locus J. Bacteriol. 192 2010 4712 4719
    • (2010) J. Bacteriol. , vol.192 , pp. 4712-4719
    • Werner, C.1    Richter, O.M.2    Ludwig, B.3
  • 65
    • 0023184331 scopus 로고
    • Bacterial evolution
    • C.R. Woese Bacterial evolution Microbiol. Rev. 51 1987 221 271
    • (1987) Microbiol. Rev. , vol.51 , pp. 221-271
    • Woese, C.R.1
  • 67
    • 66749100801 scopus 로고    scopus 로고
    • Probing structure of heme A synthase from Bacillus subtilis by site-directed mutagenesis
    • T. Mogi Probing structure of heme A synthase from Bacillus subtilis by site-directed mutagenesis J. Biochem. 145 2009 625 633
    • (2009) J. Biochem. , vol.145 , pp. 625-633
    • Mogi, T.1
  • 68
    • 28844505581 scopus 로고    scopus 로고
    • Heme A synthase enzyme functions dissected by mutagenesis of Bacillus subtilis CtaA
    • L. Hederstedt, A. Lewin, and M. Throne-Holst Heme A synthase enzyme functions dissected by mutagenesis of Bacillus subtilis CtaA J. Bacteriol. 187 2005 8361 8369
    • (2005) J. Bacteriol. , vol.187 , pp. 8361-8369
    • Hederstedt, L.1    Lewin, A.2    Throne-Holst, M.3
  • 69
    • 0036713124 scopus 로고    scopus 로고
    • Identification of novel hemes generated by heme A synthase: Evidence for two successive monooxygenase reactions
    • K.R. Brown, B.M. Allan, P. Do, and E.L. Hegg Identification of novel hemes generated by heme A synthase: evidence for two successive monooxygenase reactions Biochemistry 41 2002 10906 10913
    • (2002) Biochemistry , vol.41 , pp. 10906-10913
    • Brown, K.R.1    Allan, B.M.2    Do, P.3    Hegg, E.L.4
  • 70
    • 0033621496 scopus 로고    scopus 로고
    • Mutation of Arg-54 strongly influences heme composition and rate and directionality of electron transfer in Paracoccus denitrificans cytochrome c oxidase
    • A. Kannt, U. Pfitzner, M. Ruitenberg, P. Hellwig, B. Ludwig, W. Mantele, K. Fendler, and H. Michel Mutation of Arg-54 strongly influences heme composition and rate and directionality of electron transfer in Paracoccus denitrificans cytochrome c oxidase J. Biol. Chem. 274 1999 37974 37981
    • (1999) J. Biol. Chem. , vol.274 , pp. 37974-37981
    • Kannt, A.1    Pfitzner, U.2    Ruitenberg, M.3    Hellwig, P.4    Ludwig, B.5    Mantele, W.6    Fendler, K.7    Michel, H.8
  • 71
    • 0027738823 scopus 로고
    • Identification of the functional domains in heme O synthase. Site-directed mutagenesis studies on the cyoE gene of the cytochrome bo operon in Escherichia coli
    • K. Saiki, T. Mogi, H. Hori, M. Tsubaki, and Y. Anraku Identification of the functional domains in heme O synthase. Site-directed mutagenesis studies on the cyoE gene of the cytochrome bo operon in Escherichia coli J. Biol. Chem. 268 1993 26927 26934
    • (1993) J. Biol. Chem. , vol.268 , pp. 26927-26934
    • Saiki, K.1    Mogi, T.2    Hori, H.3    Tsubaki, M.4    Anraku, Y.5
  • 73
    • 0001888973 scopus 로고
    • Isolation and characterization of Paracoccus denitrificans mutants with increased conjugation frequencies and pleiotropic loss of a (nGATCn) DNA-modifying property
    • G.E. DeVries, N. Harms, J. Hoogendijk, and A.H. Stouthamer Isolation and characterization of Paracoccus denitrificans mutants with increased conjugation frequencies and pleiotropic loss of a (nGATCn) DNA-modifying property Arch. Microbiol. 152 1989 52 57
    • (1989) Arch. Microbiol. , vol.152 , pp. 52-57
    • Devries, G.E.1    Harms, N.2    Hoogendijk, J.3    Stouthamer, A.H.4
  • 74
    • 0028238264 scopus 로고
    • An alternative cytochrome oxidase of Paracoccus denitrificans functions as a proton pump
    • M. Raitio, and M. Wikström An alternative cytochrome oxidase of Paracoccus denitrificans functions as a proton pump Biochim. Biophys. Acta, Bioenerg. 1186 1994 100 106
    • (1994) Biochim. Biophys. Acta, Bioenerg. , vol.1186 , pp. 100-106
    • Raitio, M.1    Wikström, M.2


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